MMP9 protein (Human) (ab39308)
Constituents: 50% Glycerol, PBS, 250mM Sodium chloride, pH 7.4
Our Abpromise guarantee covers the use of ab39308 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
|Functional Studies||FuncS: Use at an assay dependent dilution. PubMed: 20422465Attenuation of the voltage-induced contraction of mouse primary cardiomyocytes.|
|SDS-PAGE||SDS-PAGE: Use at an assay dependent dilution.|
|WB||WB: Use at an assay dependent dilution. Predicted molecular weight: 92 kDa. Use at an assay dependent dilution. Predicted molecular weight: 92 kDa. Dilution optimised using Chromogenic detection. This enzyme is supplied predominantly as a zymogen, with a small amount of processed (cleaved) enzyme present. The zymogen can be activated by incubation at 37 degree Celsius for 2 to 6 hours with the organomercurial compound APMA at 1 mM. The enzyme degrades denatured collagen (gelatin), and a range of extracellular matrix components in vivo.|
- 82 kDa matrix metalloproteinase-992 kDa gelatinase92 kDa type IV collagenase
- CLG 4BCLG 4BCLG4BCollagenase Type 4 betaCollagenase Type 4 betaCollagenase type IV 92 KDCollagenase type IV 92 KDEC 184.108.40.206Gelatinase 92 KDGelatinase 92 KDGelatinase BGelatinase betaGelatinase betaGelatinaseBGELBGELBMacrophage gelatinaseMacrophage gelatinaseMANDP2Matrix metallopeptidase 9 (gelatinase B, 92kDa gelatinase, 92kDa type IV collagenase)Matrix Metalloproteinase 9Matrix Metalloproteinase 9MMP 9MMP-9MMP9MMP9_HUMANType V collagenaseType V collagenase
-Leu bond. Cleaves type IV and type V collagen into large C-terminal three quarter fragments and shorter N-terminal one quarter fragments. Degrades fibronectin but not laminin or Pz-peptide.
Metaphyseal anadysplasia 2 (MANDP2) [MIM:613073]: A bone development disorder characterized by skeletal anomalies that resolve spontaneously with age. Clinical characteristics are evident from the first months of life and include slight shortness of stature and a mild varus deformity of the legs. Patients attain a normal stature in adolescence and show improvement or complete resolution of varus deformity of the legs and rhizomelic micromelia. Note=The disease is caused by mutations affecting the gene represented in this entry.
Contains 3 fibronectin type-II domains.
Contains 4 hemopexin-like domains.
modificationsProcessing of the precursor yields different active forms of 64, 67 and 82 kDa. Sequentially processing by MMP3 yields the 82 kDa matrix metalloproteinase-9.
N- and O-glycosylated.
References for MMP9 protein (Human) (ab39308)
This product has been referenced in:
- Mishra PK et al. MMP-9 gene ablation and TIMP-4 mitigate PAR-1-mediated cardiomyocyte dysfunction: a plausible role of dicer and miRNA. Cell Biochem Biophys 57:67-76 (2010). Functional Studies . Read more (PubMed: 20422465) »
- Sans-Fons MG et al. Matrix metalloproteinase-9 and cell division in neuroblastoma cells and bone marrow macrophages. Am J Pathol 177:2870-85 (2010). Functional Studies . Read more (PubMed: 20971732) »